In vitro effects of estradiol, testosterone, and progesterone on 5-methoxyindole content, cyclic adenosine 3',5'-monophosphate synthesis, and norepinephrine release in different parts of the female guinea pig pineal complex.

To examine the effects of estradiol, testosterone, or progesterone on cyclic adenosine 3',5'-monophosphate (AMP) accumulation, 5-methoxyindole levels, and norepinephrine (NE) release by the female guinea pig pineal complex, samples of the deep, intermediate, or superficial portions of the complex were incubated in vitro with varied concentrations of either hormone. Exposure for 10 minutes to physiological amounts of estradiol (10 nM) or to 100 microM NE increased significantly cyclic AMP levels to the same extent in the three pineal regions. A maximal effect on cyclic AMP accumulation was observed at 100-nM concentrations of estradiol, with a tendency to return to basal levels at 1-10 microM of estradiol.

Application of antibody to synthetic peptides for characterization of the intact and truncated alpha 22 protein specified by herpes simplex virus 1 and the R325 alpha 22- deletion mutant.

The alpha 22 protein is one of five proteins synthesized immediately after infection of permissive cells with herpes simplex virus 1 and 2 (HSV-1 and HSV-2). On the basis of the reported nucleotide sequence of the HSV-1 gene, we synthesized two peptides containing the predicted amino acids 12 through 23 (12 residues) and 21 through 36 (16 residues) in two hydrophilic domains near the N terminus of the protein. Rabbit antisera made against these peptides were then used to characterize the alpha 22 protein made by wild-type HSV-1(F) strain and by an HSV-1 mutant, R325, carrying a 500-base-pair deletion within the coding domain of the gene.

High molecular weight lymphocyte surface proteins are structurally related and are expressed on different cell populations at different times during lymphocyte maturation and differentiation.

HMW lymphocyte surface proteins T20 and B220, which are expressed on T and B cells, respectively, have been found to be extensively related in structure, beyond what would be expected by the sharing of the determinant detected by monoclonal antibody 13/2. In addition, another HMW protein (T200A) has been discovered, which is preferentially expression proliferating T cells, and which exhibits significant structural homology with T200, but does not express the 13/2 determinant. T200A bears a novel antigenic determinant, detected by monoclonal antibody BS-S28E, which is not shared by either T200 or B220.

Melatonin increases cGMP and decreases cAMP levels in rat medial basal hypothalamus in vitro.

Measurement of cyclic nucleotide accumulation in rat medial basal hypothalamus (MBH) incubated in vitro with methoxyindoles indicated that melatonin (10(-8) M or greater) increased significantly cGMP and depressed cAMP levels. Only the effect on MBH cAMP was shared by 5-methoxytryptophol which exhibited a greater activity than melatonin. 6-Fluoromelatonin (10(-7) M) increased cGMP, whereas the effect of 6-hydroxymelatonin was not significant.

Structural differences in cell surface T25 polypeptides from thymocytes and cloned T cells.

The molecule bearing the Thy-1.2 antigen, T25, has been isolated from fractionated thymocytes as well as from cloned cytolytic and helper T cells by immune precipitation with monoclonal antibodies. Using NaDodSO4/polyacrylamide gels cross-linked with N,N'-diallytartardiamide, electrophoretic analyses of the precipitates revealed a heterogeneous pattern of polypeptide bands, ranging in apparent molecular weight from 28,000-36,000 daltons.

IgG or IgM monoclonal antibodies reactive with different determinants on the molecular complex bearing Lyt 2 antigen block T cell-mediated cytolysis in the absence of complement.

Five rat monoclonal antibodies have been derived that express specificities for determinants present on the molecular complex bearing the Lyt 2 antigen. SDS-polyacrylamide gel electrophoresis of 125I-labeled polypeptides precipitated by each of these antibodies reveal 3 components (150,000, 75,000, and 33,000 daltons), and 2 components (44,000 and 33,000 daltons) when analyzed under nonreducing and reducing conditions, respectively. Two of these antibodies are IgG and are specific for the Lyt 2.

Cell surface polypeptides of murine T-cell clones expressing cytolytic or amplifier activity.

Murine cytolytic T-cell and amplifier T-cell clones derived from secondary unidirectional mixed leukocyte cultures were labeled with 125I by the lactoperoxidase method and their polypeptide profiles were analyzed by NaDodSO4/polyacrylamide gel electrophoresis. All cytolytic T-cell clones derived from the same mouse strain yeilded similar cell surface polypeptide profiles. However, profiles obtained with three amplifier T-cell clones were strikingly different from each other as well as from those of cytolytic T-cell clones.

Brain specific creatine kinase isoenzyme behavior in rat serum after bile acid, sodium oleate and albumin injection.

In this investigation we have shown that severe liver disease with cerebral involvement can be followed by the presence of BB creatine kinase isoenzyme in serum. Groups of rats were injected with a bile acid mixture, oleic acid, albumin and normal saline respectively. Bile acids or/and oleic acid induced BB isoenzyme to leak from central nervous tissue and this can be measured in serum.

Membrane proteins specified by herpes simplex viruses. IV. Conformation of the virion glycoprotein designated VP7(B2).

The herpes simplex virus glycoprotein designated VP7(B2) is extracted from virions by nonionic detergent in the form of an oligomer, whereas the other detergent-soluble envelope proteins appear to be extracted as monomers. The subunits of the VP7(B2) oligomer cannot be dissociated by 2-mercaptoethanol and are also resistant to dissociation by a mixture of sodium dodecyl sulfate and 2-mercaptoethanol, except at elevated temperature. The oligomeric form of solubilized VP7(B2) appears to be predominantly dimeric, based on the sedimentation rats in sucrose gradients and the electrophoretic mobilities in sodium dodecyl sulfate-containing acrylamide gels of the undissociated and heat-dissociated forms of VP7(B2).

Membrane proteins specified by herpes simplex viruses. III. Role of glycoprotein VP7(B2) in virion infectivity.

Experiments done with a temperature"sensitive mutant of herpes simplex virus type 1 (HSV-1) have revealed that one of the virisn glycoproteins, designated VP7(B2), is apparently not required for the production of enveloped virus particles, whereas it does play a critical role in virion infectivity. The mutant, designated HSV-1[HFEM]tsB5, fails to accumulate VP7(B2) at nonpermissive temperature and produces virions that lack detectable quantities of this glycoprotein and that have very low specific infectivity. The poor infectivity of the virions is most readily explained by failure of penetration into the host cell rather than by failure of adsorption to cells because it was shown that the VP7(B2)-deficient virions can bind to cells and that polyethylene glycol, an agent known to promote membrane fusion, can significantly enhance infectivity of the adsorbed virions.

[Use of the serum enzymes gamma-glutamyl transpeptidase and pseudocholinesterase in hepatic pathology].

Serum gammaglutamyl transpeptidase (gammaGT) and seudocholinesterase (CHE) were studied in 20 patients with acute viral hepatitis and 36 with alcoholic cirrhosis. All had from moderate to severe clinical evolution. gammaGT is an enzyme useful to determine, as to follow clinical-biochemical evolution of viral hepatitis specially in the colestatic form.

The structural proteins and glycoproteins of herpesviruses: a review.

The virions of different herpesviruses are similar with respect to the number and kinds of constituent polypeptides, in spite of variability in the structures of individual polypeptides. The total number of virion polypeptides and glycopeptides ranges from 20 to 30 for different viruses and, in general, no more than one-quarter of these polypeptides is detectable in naked nucleocapsids, implying that most of the virion polypeptides are acquired during the process of envelopment. Although the functions of most individual structural proteins have not been identified, one can predict that the nucleocapsid proteins serve primarily structural roles or may mediate packaging of the viral genome, that the non-glycosylated envelope proteins play essential roles in the process of envelopment and that the glycoproteins, which are probably all exposed to the virion surface, mediate adsorption to and penetration of the host cell.

Comparison of the virion proteins specified by herpes simplex virus types 1 and 2.

Purified herpes simplex virus type 2 (HSV-2) virions were found to contain approximately the same number of polypeptides as HSV type 1 (HSV-1) virions. Comparisons of the structural proteins specified by five independent HSV-2 isolates revealed some minor differences in their electrophoretic profiles on sodium dodecyl sulfate-acrylamide gels; certain invariant features of the electrophoretic profiles, however, allowed clear differentiation between all the HSV-2 isolates and HSV-1.